ID   SYI_ALCBS               Reviewed;         937 AA.
AC   Q0VSE1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Isoleucyl-tRNA synthetase;
DE            EC=6.1.1.5;
DE   AltName: Full=Isoleucine--tRNA ligase;
DE            Short=IleRS;
GN   Name=ileS; OrderedLocusNames=ABO_0459;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As
CC       IleRS can inadvertently accommodate and process structurally
CC       similar amino acids such as valine, to avoid such errors it has
CC       two additional distinct tRNA(Ile)-dependent editing activities.
CC       One activity is designated as 'pretransfer' editing and involves
CC       the hydrolysis of activated Val-AMP. The other activity is
CC       designated 'posttransfer' editing and involves deacylation of
CC       mischarged Val-tRNA(Ile) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP +
CC       diphosphate + L-isoleucyl-tRNA(Ile).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: IleRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated valine is
CC       translocated from the active site to the editing site, which
CC       sterically excludes the correctly activated isoleucine. The single
CC       editing site contains two valyl binding pockets, one specific for
CC       each substrate (Val-AMP or Val-tRNA(Ile)) (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. IleS type 1 subfamily.
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DR   EMBL; AM286690; CAL15907.1; -; Genomic_DNA.
DR   RefSeq; YP_692179.1; -.
DR   GeneID; 4211348; -.
DR   GenomeReviews; AM286690_GR; ABO_0459.
DR   KEGG; abo:ABO_0459; -.
DR   NMPDR; fig|393595.12.peg.458; -.
DR   HOGENOM; Q0VSE1; -.
DR   OMA; Q0VSE1; FPMRGNL.
DR   BioCyc; ABOR393595:ABO_0459-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_02002; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR010663; DNA_glyclase/IsotRNA_synth_Znf.
DR   InterPro; IPR002301; Ile-tRNA-synt_Ia.
DR   InterPro; IPR015905; Ile-tRNA-synt_Ia_N.
DR   InterPro; IPR018353; Isoleucyl-tRNA_synthetase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR11946:SF9; Ile-tRNA-synt_Ia; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   PRINTS; PR00984; TRNASYNTHILE.
DR   TIGRFAMs; TIGR00392; ileS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    937       Isoleucyl-tRNA synthetase.
FT                                /FTId=PRO_1000022039.
FT   MOTIF        58     68       "HIGH" region.
FT   MOTIF       602    606       "KMSKS" region.
FT   METAL       900    900       Zinc (By similarity).
FT   METAL       903    903       Zinc (By similarity).
FT   METAL       920    920       Zinc (By similarity).
FT   METAL       923    923       Zinc (By similarity).
FT   BINDING     561    561       Aminoacyl-adenylate (By similarity).
FT   BINDING     605    605       ATP (By similarity).
SQ   SEQUENCE   937 AA;  104314 MW;  DB713DE4653A6E4C CRC64;
     MTDYKATLNL PQTGFPMKAG LSQREPARLK EWQQKQLYQK IREAFAGRPK FILHDGPPYA
     NGDIHIGHAV NKILKDMIVK SRTLAGFDAP YVPGWDCHGL PIELMVEKKV GKAGHKVDAG
     TFRKKCREYA SKQVAGQKSD FMRLGVLGDW DNPYLTMDFT FEANIIRSLG KIVDNGHLQQ
     GFKPVHWCLD CGSALAEAEV EYEDKISPAI DVAFPVVDVA DFVARSGIEA SAPALVIWTT
     TPWTLPANRA VAVHPELDYV LLSGELSGVA RELLVAEALA DDLVTRWGLE NVTRSAAVAG
     SKLEMLALQH PFLEAQVPVV FGEHVTTDAG TGLVHTAPGH GVDDFMVGKQ YDLDPISPVL
     DNGLFREDLP VVGGLHVSKA NEPVIEALKD SGNLVKLAKI EHSYPHCWRH KTPLIFRATA
     QWFVSMDQAG LLPRARQEID KVQWLPEWGK ARIEGMLTDR PDWCISRQRT WGVPIALFVN
     KETSELHPQT PALIEQVAQR VEKAGVDAWF DLDPAELLGD EADQYSKVTD TLDVWFDSGV
     THYCVLDQRE QLRAPADLYL EGSDQHRGWF QSSLLTSLAI RDAAPYSTVL THGFTVDEHG
     RKMSKSVGNV IAPQEVWNDL GADILRLWVC ATDYRGEMSV SKDILKQMGD SYRRIRNTSR
     FLLSNLSGFE PATDALQPEQ MLALDRYIVD RALQVQAEIQ DLYDGYHFHQ VYQKLHNFCA
     LDLGGFYLDI IKDRQYTTQA DSVARRSCQT ALYHIAQALV RWMAPVLSFT AEEIYENLPG
     ERLDSVFLAE WYDGLFALAD NADMGRAFWD KVQDAKQAVN KAIEGARAAK LIKGSLSAEV
     VLFVDAEQNA LLQRLGDELR FVTITSAAVL KPLAEAPAEL EDTSVAGLKV QVLASDHAKC
     ARCWHHQPDV GSHAEHPELC GRCITNVEGD GEVRHYA
//